Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027651 (tumor)
 685,946 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Early detection is still the most urgent concern for the successful treatment of carcinoma of the thyroid. A considerable obstruction to early tumor recognition in Germany is the still much too frequently recorded "endemic goiter". A consistent general goiter prophylaxis by iodization of the domestic salt may also have a favorable influence on tumor diagnosis. The basis for an exhaustively planned treatment of "struma maligna" is the histomorphological classification of tumors. By radical surgical intervention and the selective application of isotope and megavolt irradiation and obligatory prescription of thyroid hormone the treatment results, especially in the differentiated thyroid carcinomata, can be improved to 10-year survival rates of more than 85%.
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PMID:[Therapy of malignant tumors of the thyroid]. 40 38

Cytosol obtained from cryptorchid testes of tumor-susceptible BALB/c and resistant C3HBi (Z) mice both bound 17 beta-estradiol (E2) and diethylstilbestrol (DES) specifically. The dissociation constant (Kd) of this binding component (RE) for E2 was determined to approximate 5 x 10(-9) M. Gel filtration of cytosols resulted in a significant increase in the binding constant (Kd approximately 3 x 10(-10) M) with the majority of the complex migrating in the 7-8S area after sucrose gradient centrifugation. Incubation of either untreated or gel-filtered cytosol with [3H]DES resulted in considerable nonspecific binding appearing in the 4S region in a low salt sucrose gradient. This 4S binding of [3H]DES was not inhibited by the addition to the incubation mixtures of a 100-fold excess of either E2 or DES, while the lesser peak at 7-8S as well as the major 7-8S peak formed with E2 were inhibited by both. In vitro translocation of the cytosol RE to the nucleus was demonstrated in both mouse strains using either estrogen. Quantitation of the in vivo translocation, employing the exchange method after a single injection of 2.5 micrograms E2/mouse, revealed a rapid increase in cytoplasmic receptor content accompanied by a concomitant increase in nuclear receptor content. Greater nuclear receptor content was identified in nuclei from BALB/c mice than in those from Z animals 45 min after injection of E2. The binding behavior of E2-RE complexes to nuclei was studied by the KCl extraction method. The percent extracted from the nuclei in the Z strain was significantly greater than that in the BALB/c at all concentrations of KCl tested. Essentially 100% of the RE was extracted from nuclei of Z animals at 0.4 M KCl, while nuclei of BALB/c mice retained 35-40% even in 2 M KCl. Cross-over experiments in a cell-free system suggested that the difference in binding was due to differences in chromatins rather than in nuclear estrogen-receptor complexes. The greater nuclear receptor content and stronger binding of nuclear receptor to chromatin might explain why estrogen-induced phenomena, including neoplastic transformation occur to a much greater degree in the BALB/c strain than in the Z strain of the mouse.
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PMID:The testicular estrogen receptor system in two strains of mice differing in susceptibility to estrogen-induced Leydig cell tumors. 43 39

The size of androgen receptors from rat ventral and dorsal prostate, dorsal prostate (Dunning) tumor, testis, epididymis, and seminal vesicle was determined using Sephadex G-200 chromatogrpahy and sucrose gradient centrifugation. The protease inhibitor diisopropyl fluorophosphate (DFP) was used to minimize receptor breakdown. An 8-9 S, 85 to 106 A receptor (Mr = 280,000 to 365,000; f/fo = 1.9 to 2.4) observed in unfractionated cytosol prepared in low ionic strength buffer with or without DFP is in equilibrium with a 4.5-5 S, 58 A form (Mr = 117,000; f/fo = 1.8) observed at salt concentrations greater than 0.1 M KCl. Receptor partially purified using (NH4)2SO4 or phosphocellulose chromatography in the absence of DFP was present as smaller fragments of 3.6 S, 37 A and 3.0 S, 23 A. Similar fragments could be generated from the 4.5 S or 8 S receptor by mild trypsin treatment. In addition, ventral prostate contains a DFP-insensitive enzyme which specifically converts the 4.5 S, 58 A receptor to the 3.6 S 37 A fragment. The DFP-insensitive enzyme is partially inhibited by rabbit bile and appears similar to the enzyme seminin, a secretory protein of human prostate. Androgen receptor isolated in the presence of DFP from nuclei labeled in vivo is predominantly 4.5 S, 58 A, with smaller forms (37 and 23 A) appearing in the absence of DFP. The 4.5 S, 58 A nuclear receptors were also in equilibrium with a large 8 S form. Receptor breakdown by DFP-insensitive and sensitive proteases appears to be an in vitro phenomenon. Furthermore, the size of the androgen receptor is not significantly changed during receptor migration from cytoplasm to nucleus.
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PMID:Effects of proteases and protease inhibitors on the 4.5 S and 8 S androgen receptor. 44 15

The physicochemical properties of nuclear and cytosolic glucocorticoid-binding components from corticoid-sensitive (CS) and corticoid-resistant (CR) mouse lymphoma P1798 cells have been compared. Nuclei or cytosol fractions were prepared from lymphocytes that had been labeled at 37 or 4 degrees, respectively, with 30 nM [3H]triamcinolone acetonide ([3H]TA). [3H]TA was extracted with 0.6 M KCl, 10 mM spermidine, or 4.5 mM MgCl2 from CS nuclei and with 0.6 M KCl or 10 mM spermidine from CR nuclei. As reported previously, nuclear-associated [3H]TA in CR cells was resistant to extraction with mM concentrations of MgCl2. Loss of bound steroid during extraction with 0.6 M KCl was minimized by including the chymotrypsin inhibitor, carbobenzoxy-L-phenylalanine, in the extraction buffer. The inhibitor was not required during extraction with spermidine or MgCl2. Nuclear and cytosolic extracts were examined by analytical agarose gel filtration and glycerol density gradient centrifugation under high salt (0.6 M KCl) conditions. The glucocorticoid-binding component in KCl, spermidine, and MgCl2 extracts from CS nuclei was considerably larger and more asymmetrical [Stokes radius, 57 to 59 A; sedimentation coefficient, 3.64 to 3.70S; molecular weight, 90,000 daltons; frictional ratio, 1.8; axial ratio (prolate ellipsoid), 15] than the [3H]TA-macromolecular complex in KCl and spermidine extracts from CR nuclei[Stokes radius, 29 A; sedimentation coefficient, 3.23 to 3.30S; molecular weight, 40,000 daltons; frictional ratio, 1.25; axial ratio (prolate ellipsoid), 5]. Control experiments showed that the smaller size of the glucocorticoid-binding component in CR nuclei was probably not due to cleavage of a larger, CS-like complex during the extraction procedure. The larger size of the CS [3H]TA complex did not appear to result from aggregation of s a smaller species. No difference in physicochemical parameters of the binding component was observed if cells were labeled with [3H]dexamethasone instead of [3H]TA. However, [3H]dexamethasone complexes were less stable than those formed with [3H]TA as indicated by considerable dissociation of [3H]dexamethasone during gel filtration and gradient centrifugation. This may be due to the 3- to 5-fold lower relative binding affinity of [3H]dexamethasone. Analysis of [3H]TA-labeled cytosol by gel filtration and gradient centrifugation revealed the presence of a single binding component with physicochemical properties similar to those of nuclear [3H]TA complexes from the same strain of tumor. These results suggest that previously described differences in extractability of nuclear-associated [3H]TA between the CS and CR strains of mouse lymphoma P1798 and the lack of response of CR P1798 to glucocorticoid administration may be due, at least in part, to the presence of an altered glucocorticoid-binding component in the resistant tumor cells.
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PMID:Physicochemical differences between glucocorticoid-binding components from the corticoid-sensitive and -resistant strains of mouse lymphoma P1798. 47 39

This study was undertaken to explore the effects of chronic low-level cadmium ingestion in Dahl hypertension-resistant (R) and hypertension-sensitive (S) lines of rats. Groups of weanling female R and S rats were given 0 or 1 mg cadmium/1. in drinking water and fed either a low salt (0.4% NaCl) or a high salt (4% NaCl) diet for 28 weeks. Cadmium produced hypertension associated with gross cardiac hypertrophy and mild to moderate renal vascular changes in S, but not in R, rats on a low salt diet. Cadmium enhanced the rate and degree of development of salt-induced hypertension without exacerbating the hypercholesterolemia or renal vascular lesions normally observed in S rats on a high salt diet. Cadmium lowered circulating cholesterol levels in both lines on a low salt diet. Cadmium had no influence on growth, blood urea nitrogen concentration, plasma renin activity, tumor formation, or survivorship in R and S rats on either salt diet. This study indicates that the genetic composition is a critical determinant of the adverse effects of chronic low-level cadmium ingestion in rats. In addition to the experimental implications, these findings may have relevance to the problem of human "essential" hypertension.
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PMID:Effects of cadmium ingestion in rats with opposite genetic predisposition to hypertension. 48 40

When partially purified Ehrlich ascites tumor RNA polymerase II was further purified on a column of phosphocellulose, stimulation of its catalysis of RNA synthesis by stimulatory factor S-II was greatly decreased. This decrease in sensitivity to the stimulatory factor was reversible: the enzyme eluted from phosphocellulose became sensitive to the factor when mixed with a protein fraction eluted from the phosphocellulose at high salt concentration. Evidence was obtained that this protein, named helper protein, binds, to the enzyme eluted from phosphocellulose, causing it to recover sensitivity to stimulatory factor S-II.
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PMID:Protein which interacts with a stimulatory factor of RNA polymerase II of Ehrlich ascites tumor cells. 56 40

Estrogens stimulate prolactin (PRL) synthesis by GH3 cells, a clonal strain of rat pituitary cells grown in culture. At 4 degrees C the binding of [3H]17 beta-estradiol to monolayer cultures of GH3 cells was specific and of limited capacity, with half-maximal and maximal binding after 1--2 h and 12 h, respectively. Scatchard analysis showed one single class of binding sites with Kd = 3.1 X 10(-10) M and n = 309 X 10(-15) mol 17 beta-estradiol/mg cell protein, calculated to give approx. 25,000 binding sites per cell. At 4 degrees C less than 10% of the specifically bound [3H]17 beta-estradiol was found in the nuclear fraction. When the incubation temperature was raised to 37 degrees C, the amount of radioactivity in the nucleus increased to 25% within 30 min with a corresponding reduction in the cytoplasm. The cytosol fractions from monolayer cultures as well as from tumors of GH3 cells contained specific 17 beta-estradiol binding proteins, having a sedimentation constant close to 8S in a salt-free buffer and 4S in the presence of 0.5 M KCl. scatchard analysis showed one single class of binding sites with Kd = 3.6 X 10(-10) M and n = 258 X 10(-15) mol 17 beta-estradiol/mg cytosol protein (GH3 tumor tissue). Thus, GH3 cells grown in culture and in the intact animal have similar binding characteristics as judged from the data for binding affinity, capacity and specificity. After the in vivo administration of [3H]17 beta-estradiol to GH3 tumor-bearing rats, radioactivity could be extracted (0.5 M KCl) from purified nuclei bound to 4.5S macromolecules. We suggest that the action of 17 beta-estradiol on GH3 cells involves an initial binding of the steroid to specific receptors in the cytoplasm, followed by transport of a fraction of the hormone-receptor complexes to the nucleus involving a temperature-sensitive step.
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PMID:Receptors for 17beta-estradiol in prolactin-secreting rat pituitary cells. 56 89

Tumor tissue of cutaneous fibrosarcoma was solubilized with salt, acetic acid and salt-extracted after pepsin treatment. Type III collagen was observed in neutral soluble collagen, 1.5 M and 2.4 M NaCl precipitated fractions after pepsin treatment. Type III collagen fraction precipitated with 1.5 M NaCl eluted in the alpha2 region when chromatographed on CM-cellulose without reduction, while the type III collagen partially purified with 1.5 M NaCl eluted between the position of alpha1(I) and beta12 after reduction and alkylation. Analysis of amino acid showed the presence of cysteine and the high content of hydroxyproline following CM-chromatography of 1.5 M NaCl precipitated type III collagen fraction. Acidic glycosaminoglycans were composed of hyaluronic acid, chondroitin sulfate, dermatan sulfate and heparan sulfate, and the first two were major components of fibrosarcoma.
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PMID:Biochemical characterization of connective tissue macromolecules derived from cutaneous fibrosarcoma. 59 35

Daunomycin was coupled via its amino group to omega-carboxypentyl agarose (CH-Sepharose 4B). Nonhistone proteins from rat leukemia cells (DBLA-6) were fractionated on a column of the adsorbent. The adsorption of nonhistone proteins to the column was increased by high salt concentration (4 M NaCl) and was reversed by 20% glycerol (v/v), indicating a hydrophobic interaction. Complexity of the chromatographic patterns may reflect the occurrence of several species of binding protein in the tumor cells used. Thus the hydrophobic chromatography in the presence of a high concentration of salt was a useful method for fractionation of nonhistone proteins under non-rigorous conditions.
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PMID:Fractionation of nonhistone proeins on a column of daunomycin-CH-Sepharose 4B. 62 48

Hypertonic salt extracts (3 M KCl) of x-irradiation-induced Holtzman rat small bowel adenocarcinomas blocked the in vitro destruction of allogeneic cultured cells of this malignancy by sensitized lymphoid cells obtained from tumor-bearing animals. The protective effect were mediated by a blocking action at both the effector and the target cell level. The extracts were separated into 50% ammonium sulfate soluble and insoluble fractions with the soluble fraction being more effective in blocking the cytotoxic responses through interaction with the lymphoid cells whereas the insoluble one had a greater effect upon tumor target cells. Associated with both fractions was the oncofetal glycoprotein previously identified with the cellular membrane of this x-ray-induced malignancy. Immunoglobulins were identified with insoluble fraction; some were able to bind the oncofetal protein, thus clasifying it as a fetal antigen. The protective effects of the soluble fraction and this neoantigen were found to be citric acid labile, whereas the effects due to the insoluble fraction were unchanged.
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PMID:Lymphocyte cytotoxicity in x-irradiation-induced rat small bowel adenocarcinoma. III. Blocking by 3 M KCL extract. 62 24


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